Studies on Ca2+Binding of Thermostable α-Amylase

Abstract

Abstract: It was determined that α-amylase contained ten Ca²⁺.Resulted from the study of stability and activity of Ca²⁺-free α-amylase after adding Ca²⁺, the first eight Ca²⁺related to catalytic function of the enzyme, the other two Ca²⁺made the structure of enzyme stable. According to the CDand fluorescence spectra of α-amylase at room temperature, no significant change of the enzyme structure was observed. Furthermore, according to the CDspectra of α-amylase after adding Ca²⁺(heated at 90 ℃ for 15 min), some α-helix structures of the enzyme still existed. Fluorescence spectra of α-amylase at 90 ℃ for 15 min also showed that enzyme kept the conformation maximum stability when the Ca²⁺-free α-amylase was binding to 10 Ca²⁺.All the results indicated that the dependence of enzyme conformation on Ca²⁺was low.

Key words: α-Amylase,Ca²⁺, Conformation

CLC Number:

Q93.936

TrendMD:

ZHAO Ying, FEI Xiao-Fang, ZHENG Yu-Juan, DONG Qing-Chu, WANG Jie, CHENG Gang. Studies on Ca²⁺Binding of Thermostable α-Amylase[J]. Chem. J. Chinese Universities, 1998, 19(8): 1267.

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Studies on Ca²⁺Binding of Thermostable α-Amylase

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